Loss of mitofusin 2 promotes endoplasmic reticulum stress. - Wikidata - awgldk - TriplyDB

Loss of mitofusin 2 promotes endoplasmic reticulum stress.

Loss of mitofusin 2 promotes endoplasmic reticulum stress.

http://www.wikidata.org/entity/Q36016910

about

p58IPK is an inhibitor of the eIF2α kinase GCN2 and its localization and expression underpin protein synthesis and ER processing capacity Mitochondrial Quality Control and Muscle Mass Maintenance Functional implications of mitofusin 2-mediated mitochondrial-SR tethering Dengue Virus Impairs Mitochondrial Fusion by Cleaving Mitofusins Muscle-specific Drp1 overexpression impairs skeletal muscle growth via translational attenuation.The diabetes susceptibility gene Clec16a regulates mitophagy Mfn2 modulates the UPR and mitochondrial function via repression of PERK Mitofusins and the mitochondrial permeability transition: the potential downside of mitochondrial fusion Mitochondrial fusion but not fission regulates larval growth and synaptic development through steroid hormone production.Mitochondrial hyperfusion during oxidative stress is coupled to a dysregulation in calcium handling within a C2C12 cell model.Calcium trafficking integrates endoplasmic reticulum function with mitochondrial bioenergetics PINK1 deficiency impairs mitochondrial homeostasis and promotes lung fibrosis.Mitochondrial dynamics in pulmonary arterial hypertension.Dissociation of mitochondrial from sarcoplasmic reticular stress in Drosophila cardiomyopathy induced by molecularly distinct mitochondrial fusion defects.Mitochondrial dynamics protein Drp1 is overexpressed in oncocytic thyroid tumors and regulates cancer cell migration Low Expression of Mfn2 Is Associated with Mitochondrial Damage and Apoptosis of Ovarian Tissues in the Premature Ovarian Failure Model Mice Hemizygous for a Pathogenic Mitofusin-2 Allele Exhibit Hind Limb/Foot Gait Deficits and Phenotypic Perturbations in Nerve and Muscle Mitofusins 1 and 2 are essential for postnatal metabolic remodeling in heart The Association of Mitofusion-2 Gene Polymorphisms with Susceptibility of Essential Hypertension in Northern Han Chinese Population.New concepts of endoplasmic reticulum function in the heart: programmed to conserve.Mitochondrial dynamics in the adult cardiomyocytes: which roles for a highly specialized cell?Autophagy: an affair of the heart Mitofusin 2 in POMC neurons connects ER stress with leptin resistance and energy imbalance.Mitofusin 2 maintains haematopoietic stem cells with extensive lymphoid potential.Mitochondrial oxidative phosphorylation controls cancer cell's life and death decisions upon exposure to MAPK inhibitors.Junctophilin 3 expresses in pancreatic beta cells and is required for glucose-stimulated insulin secretion.Reduction of endoplasmic reticulum stress attenuates the defects caused by Drosophila mitofusin depletion.Mitochondrial fusion and fission proteins: novel therapeutic targets for combating cardiovascular disease.Mitochondrial-Shaping Proteins in Cardiac Health and Disease - the Long and the Short of It!Dysregulation of Mfn2 and Drp-1 proteins in heart failure.Proteostasis control by the unfolded protein response Role of Endoplasmic Reticulum-Mitochondria Communication in Type 2 Diabetes.The SAT Protein of Porcine Parvovirus Accelerates Viral Spreading through Induction of Irreversible Endoplasmic Reticulum Stress.The coming of age of the mitochondria-ER contact: a matter of thickness.Endoplasmic reticulum proteostasis in hepatic steatosis.Loss of mitofusin 2 links beta-amyloid-mediated mitochondrial fragmentation and Cdk5-induced oxidative stress in neuron cells.Mitochondrial Dynamics as a Therapeutic Target for Treating Cardiac Diseases.P58(IPK) inhibits coxsackievirus-induced apoptosis via the PI3K/Akt pathway requiring activation of ATF6a and subsequent upregulation of mitofusin 2.The Unfolded Protein Response: At the Intersection between Endoplasmic Reticulum Function and Mitochondrial Bioenergetics Assessing the effects of mitofusin 2 deficiency in the adult heart using 3D electron tomography.

P2860

Q24306090-140D009F-7549-46F6-92B7-4273A326EAF9 Q26770420-29C7541C-D696-43A5-87CE-CFCBF8594165 Q27025868-C1F80580-1536-442A-870A-F7A1CC9BE23D Q27316360-04059D60-668E-41A4-BB48-40CE48AB52ED Q27330378-42319E7D-1B0D-47EB-A4EF-9F523F53C47F Q28511990-5F6522EC-8498-4052-AB83-4F74CA93A02F Q28589398-DD1C7F27-81F1-41E9-B5CE-B0C36ED5675D Q34277591-562EBA5E-E457-4B5D-94AF-016FF6BF742E Q34432596-A405BF33-77C8-49DB-850C-EBF5E380896E Q34828427-B31ED68F-B5BD-446D-8A1E-482A1590B2F0 Q34841551-39B1AD4F-C050-4AEB-9B54-56FB68D87582 Q35056685-9F3A7ED0-88A8-484F-9E5B-125ABEBA60D4 Q35116543-666AE95F-9B7A-4C3F-86CD-E43D6DA11D8E Q35137604-38E5A748-E0CE-4346-BB45-C3C9A0E8BA0B Q35231712-0C94AFE4-E03E-40ED-AEF4-7BD0543E49E1 Q35761172-0F792C0A-A256-4C85-8243-561D21D06492 Q36210125-09DAC0EA-DA2A-4298-9AF5-D03E071DF99E Q36455449-1F0AB39D-9416-46C0-86D3-5074BBCAE526 Q36473802-360C9111-396E-4885-B86B-A5BC9326D126 Q36570092-5C76AA06-A355-444C-A899-FE756F0CD136 Q36833311-06268CAA-952B-414C-AF6C-0E2FF2FB98D2 Q37196353-6583B08B-83C9-4BAE-8D43-FD45FF9227FD Q37339111-11183C9D-FFC3-4FEB-B933-91072EBFF940 Q37410531-859770A5-B433-4150-BB75-09EFCD30FCB7 Q37457568-B30AD076-8053-4528-92B1-96F911675D77 Q37482839-3DD3C753-E390-4B53-86C7-72E3A5728D2C Q37550651-BC9EEEC8-4172-41B7-8574-69B41A971379 Q37686255-D0BA45CE-C2D5-4211-83FF-938507772876 Q37694547-11944E1B-F581-40F6-8410-D8BEB7A21258 Q38218183-6A0C5B88-B414-4A06-B028-D66F718A9163 Q38540196-616864E6-E02D-430C-8D2D-3B3C87B72106 Q38620972-1AEADA51-8754-4EC4-9129-C74B17862A87 Q38701700-E16FFE37-0F37-475F-A97A-BEC4583A9FA3 Q38875975-BF31F846-8E56-4749-9827-B4807BDE026F Q38925531-CC6D97BE-551E-47CE-8095-CCDC2262B91E Q38943638-445763D2-9147-45C9-BB92-63BA4ADCBB57 Q39008813-1980CE90-67F9-4989-B119-53278432D966 Q39077521-146897F5-5FD2-4EBE-8DBD-EFD4EA2D12EC Q39249695-25D8FC4F-6516-4C65-961E-DBD2D0CA6137 Q41037443-987BEDC6-0567-420F-970C-41ECB7C6E503

P2860

Loss of mitofusin 2 promotes endoplasmic reticulum stress.

http://www.wikidata.org/entity/Q36016910

description

2012 nî lūn-bûn

@nan

2012年の論文

@ja

2012年学术文章

@wuu

2012年学术文章

@zh-cn

2012年学术文章

@zh-hans

2012年学术文章

@zh-my

2012年学术文章

@zh-sg

2012年學術文章

@yue

2012年學術文章

@zh

2012年學術文章

@zh-hant

name

Loss of mitofusin 2 promotes endoplasmic reticulum stress.

@ast

Loss of mitofusin 2 promotes endoplasmic reticulum stress.

@en

type

label

Loss of mitofusin 2 promotes endoplasmic reticulum stress.

@ast

Loss of mitofusin 2 promotes endoplasmic reticulum stress.

@en

prefLabel

Loss of mitofusin 2 promotes endoplasmic reticulum stress.

@ast

Loss of mitofusin 2 promotes endoplasmic reticulum stress.

@en

P1433

Q36016910-E67E6718-6329-4740-8F91-41A6A2588ABF

P1476

Q36016910-7BB93D51-C5B8-45BB-9235-363B19203F08

P2093

Q36016910-31B1C237-0F7F-4B12-B659-16C4C311CEC5

Q36016910-6F717FB7-364A-4112-8479-425E12541760

Q36016910-A8CDE8CB-B728-4B91-93DC-D45647968E0D

P2860

Q36016910-027447E5-1941-426B-8E51-76E217EBABB1

Q36016910-0BB233F4-6C4F-413A-B747-24957BC07A75

Q36016910-0C3C224F-881E-4F84-8A60-76A0B0EC6E3E

Q36016910-13AFFB96-5A4A-4309-888D-86C57DC21115

Q36016910-192D11B6-BF2D-4EC8-84F8-60548836AACC

Q36016910-1A56BEBB-9D16-4C96-B868-2A59B8C93B7E

Q36016910-1ECD3F94-45A5-44F4-BAF3-0A8593C42E4B

Q36016910-29838DA3-BC11-49C3-BB12-57E004CBAB96

Q36016910-2E39EE16-77D2-483E-85D6-8616E50DBC30

Q36016910-2F4FBAEA-A6C6-47B7-A584-79B3ED4CBC94

P304

Q36016910-A8968E3B-1252-463D-BDE8-4EA49275DAAC

P31

Q36016910-6BB20454-FE23-4EDA-822B-808B95689E84

P356

Q36016910-674A4360-E7BA-4FAD-8709-CFFBF156D891

P407

Q36016910-B0DFF9E6-3930-402D-84E1-0AA23D6F0DE8

P433

Q36016910-94F07F64-0A85-452E-8FE5-0CC3FF1F4A8E

P478

Q36016910-7D6C9B16-72E2-4320-AA48-559EFE3C0106

P577

Q36016910-36A4B331-BDBB-4137-B51D-17F6205C2E66

P698

Q36016910-1AE3A31C-3A96-4F86-8B29-D23135A3370B

P921

Q36016910-3F35E689-695F-4460-9CC5-55392DCDB31C

P932

Q36016910-55546979-65C7-48D3-ADBA-1BCBD0DEB3AC

P356

JBC.M112.359174

P1433

Journal of Biological Chemistry

P1476

Loss of mitofusin 2 promotes endoplasmic reticulum stress.

@en

P2093

Gladys A Ngoh

http://www.w3.org/2001/XMLSchema#string

Kenneth Walsh

http://www.w3.org/2001/XMLSchema#string

Kyriakos N Papanicolaou

http://www.w3.org/2001/XMLSchema#string

P2860

Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors

Control of mitochondrial morphology by a human mitofusin

Endoplasmic reticulum stress: cell life and death decisions.

Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK.

An intimate liaison: spatial organization of the endoplasmic reticulum-mitochondria relationship

Signal integration in the endoplasmic reticulum unfolded protein response

Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation

EIF2AK3, encoding translation initiation factor 2-alpha kinase 3, is mutated in patients with Wolcott-Rallison syndrome

Translational control is required for the unfolded protein response and in vivo glucose homeostasis

Intracellular signaling by the unfolded protein response

P304

20321-20332

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.M112.359174

http://www.w3.org/2001/XMLSchema#string

P407

P433

24

http://www.w3.org/2001/XMLSchema#string

P478

287

http://www.w3.org/2001/XMLSchema#string

P577

2012-04-17T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

22511781

http://www.w3.org/2001/XMLSchema#string

P921

endoplasmic reticulum

P932

3370214

http://www.w3.org/2001/XMLSchema#string